Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5R880

- PLA2R_PONAB

UniProt

Q5R880 - PLA2R_PONAB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Secretory phospholipase A2 receptor

Gene

PLA2R1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Receptor for secretory phospholipase A2 (sPLA2). Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow-derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B and sPLA2-X/PLA2G10 (By similarity).By similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. phospholipase binding Source: UniProtKB
  3. receptor activity Source: UniProtKB

GO - Biological processi

  1. cytokine production Source: UniProtKB
  2. oxidative stress-induced premature senescence Source: UniProtKB
  3. positive regulation of arachidonic acid secretion Source: UniProtKB
  4. positive regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  5. reactive oxygen species metabolic process Source: UniProtKB
  6. receptor-mediated endocytosis Source: UniProtKB
  7. replicative senescence Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Secretory phospholipase A2 receptor
Short name:
PLA2-R
Short name:
PLA2R
Alternative name(s):
180 kDa secretory phospholipase A2 receptor
M-type receptor
Cleaved into the following chain:
Soluble secretory phospholipase A2 receptor
Short name:
Soluble PLA2-R
Short name:
Soluble PLA2R
Gene namesi
Name:PLA2R1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 13981376ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1399 – 141921HelicalSequence AnalysisAdd
BLAST
Topological domaini1420 – 146445CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222By similarityAdd
BLAST
Chaini23 – 14641442Secretory phospholipase A2 receptorPRO_0000311252Add
BLAST
Chaini23 – ?Soluble secretory phospholipase A2 receptorBy similarityPRO_0000311253

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 66By similarity
Disulfide bondi91 ↔ 108By similarity
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi180 ↔ 206By similarity
Disulfide bondi194 ↔ 221By similarity
Disulfide bondi262 ↔ 356By similarity
Disulfide bondi332 ↔ 348By similarity
Disulfide bondi408 ↔ 503By similarity
Glycosylationi456 – 4561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi480 ↔ 495By similarity
Disulfide bondi619 ↔ 636By similarity
Disulfide bondi701 ↔ 798By similarity
Disulfide bondi776 ↔ 790By similarity
Disulfide bondi842 ↔ 939By similarity
Disulfide bondi916 ↔ 931By similarity
Disulfide bondi1069 ↔ 1089By similarity
Disulfide bondi1211 ↔ 1225By similarity
Disulfide bondi1282 ↔ 1378By similarity
Disulfide bondi1356 ↔ 1370By similarity

Post-translational modificationi

The secretory phospholipase A2 receptor form may be produced by the action of metalloproteinases. It contains all extracellular domains and only lacks transmembrane and cytosolic regions. It is however unclear whether this form is produced by proteolytic cleavage as suggested by some experiments, or by alternative splicing (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5R880.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 163124Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini175 – 22349Fibronectin type-IIPROSITE-ProRule annotationAdd
BLAST
Domaini240 – 357118C-type lectin 1PROSITE-ProRule annotationAdd
BLAST
Domaini387 – 504118C-type lectin 2PROSITE-ProRule annotationAdd
BLAST
Domaini524 – 645122C-type lectin 3PROSITE-ProRule annotationAdd
BLAST
Domaini675 – 799125C-type lectin 4PROSITE-ProRule annotationAdd
BLAST
Domaini821 – 940120C-type lectin 5PROSITE-ProRule annotationAdd
BLAST
Domaini967 – 1098132C-type lectin 6PROSITE-ProRule annotationAdd
BLAST
Domaini1123 – 1234112C-type lectin 7PROSITE-ProRule annotationAdd
BLAST
Domaini1259 – 1379121C-type lectin 8PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1437 – 14437Endocytosis signal

Domaini

C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B.By similarity
The endocytosis signal probably mediates endocytosis via clathrin-coated pits.By similarity

Sequence similaritiesi

Contains 8 C-type lectin domains.PROSITE-ProRule annotation
Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG108261.
InParanoidiQ5R880.
KOiK06560.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
[Graphical view]
SMARTiSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
PROSITEiPS00615. C_TYPE_LECTIN_1. 3 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5R880-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLSPSLLLP LLLLLGAPRG CAEGVAAALT PERLLEWQDK GIFVIQSESL
60 70 80 90 100
KKCIQAGKSV LTLENCKQAN KHMLWKWVSN HGLFNIGGSG CLGLNFSAPE
110 120 130 140 150
QPLSLYECDS TLVSLRWRCD RKMITGPLQY SVQVAHDNTV VASRKYFHKW
160 170 180 190 200
ISYGSGGGDI CEYLHKDLHT IKGNAHGMPC MFPFQYNHQW HHECTREGRE
210 220 230 240 250
DDLLWCATTS RYERDEKWGF CPDPTSAEVG CDTIWEKDLN SHICYQFNLL
260 270 280 290 300
SSLSWSEAHS SCQMQGGALL SITDETEENF IREHMSSKTV EVWMGLNQLD
310 320 330 340 350
EHAGWQWSDG TPLNYLNWSP EVNFEPFVED HCGTFSSFIP SAWRSRDCAS
360 370 380 390 400
TLPYVCKKYL NHIDHEIVEK DAWKYYATHC EPGWNPYNRN CYKLQKEEKT
410 420 430 440 450
WHEALRSCQA DNSALIDITS LAEVEFLVTL LGDENASETW IGLSSNKIPV
460 470 480 490 500
SFEWSNDSSV IFTNWHTLEP QIFPNRSQLC VSAEQSEGHW KVKNCEETLF
510 520 530 540 550
YVCKKAGHVL SDAESGCQEG WERHGGFCYK IDTVLRSFDQ ASSGYYCPPA
560 570 580 590 600
LVTITNRFEQ AFITSLIGSV VKMKDSYFWI ALQDQNDTGE YTWKPAGQKP
610 620 630 640 650
EPVQYTHWNA HQPRYSGGCV AMRGRHPPGR WEVKHCRHFK AMSLCKQPVE
660 670 680 690 700
NQEKAEYEER WPFHPCYLDW ESEPGLASCF KVFHSEKVLM KRTWREAEAF
710 720 730 740 750
CEEFGAHLAS FAHIEEENFV NELLYSKFNW TEERQFWIGF NKRNPLNAGS
760 770 780 790 800
WEWSDRIPVV SSFLDNNYFG EDARNCAVYK ANKTLLPLHC GSKREWICKI
810 820 830 840 850
PRDVKPKIPF WYQYDVPWLF YQDAEYLFHT FASEWLNFEF VCSWLHSDLL
860 870 880 890 900
TIHSAHEQEF IHSKIKALSK YGASWWIGLQ EERANDEFRW RDGTPVIYQN
910 920 930 940 950
WDTGRERPVN NQSQRCGFIS SITGLWGSEE CSVSMPSICK RKKVLLIEKK
960 970 980 990 1000
KDTPKQHGTC PKGWLYFNYK CLLLNIPKDP NSWKNWMHAQ HFCAEEGGTL
1010 1020 1030 1040 1050
VAIESEVEQA FITMNLFGQT TNVWIGLQND DYETWLNGKP VVYSNWSPFD
1060 1070 1080 1090 1100
IINIPSHNTT DVQKHIPLCA LLSSNPNFHF TGKWYFEDCG KEGYGFVCEK
1110 1120 1130 1140 1150
MQDTSGHGVN TSDMYPMPNT LEYGNRTYKI INANMTWYAA IKTCLMHGTQ
1160 1170 1180 1190 1200
LVSITDQYHQ SFLTVVLNRL GYAHWIGLFT TDNGLNFDWS DGTKSSFTFW
1210 1220 1230 1240 1250
KDEESSLLGD CVFADTNGLW HSTACESFLQ GAICHVPPET RQSEHPELCS
1260 1270 1280 1290 1300
ETSIPWIKFK SNCYSFSTVL DRMSFEAAHE FCKKEGSNLL TIKDEAENAF
1310 1320 1330 1340 1350
LLEELFAFGS SVQMVWLNAQ FDGNNETIKW FDGTPTDQSN WGIRKPDTDY
1360 1370 1380 1390 1400
FKPHHCVALR IPEGLQLSLC QEKKGFICKM EADIRTAEEL PEKGPSHSII
1410 1420 1430 1440 1450
PLAVVLTLIV IVAICTLSFC IYKHNGGFFR RLAGFRNPYY PATNFSTVHL
1460
EENILISDLE KSDQ
Length:1,464
Mass (Da):168,437
Last modified:November 13, 2007 - v2
Checksum:i8D4DEA5A43CB1C8A
GO

Sequence cautioni

The sequence CAH92030.1 differs from that shown. Reason: Erroneous termination at position 1366. Translated as Gln.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR859874 mRNA. Translation: CAH92030.1. Sequence problems.
RefSeqiNP_001126180.1. NM_001132708.1.
UniGeneiPab.11399.

Genome annotation databases

GeneIDi100173143.
KEGGipon:100173143.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR859874 mRNA. Translation: CAH92030.1 . Sequence problems.
RefSeqi NP_001126180.1. NM_001132708.1.
UniGenei Pab.11399.

3D structure databases

ProteinModelPortali Q5R880.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100173143.
KEGGi pon:100173143.

Organism-specific databases

CTDi 22925.

Phylogenomic databases

HOVERGENi HBG108261.
InParanoidi Q5R880.
KOi K06560.

Family and domain databases

Gene3Di 2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
[Graphical view ]
SMARTi SM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
PROSITEi PS00615. C_TYPE_LECTIN_1. 3 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiPLA2R_PONAB
AccessioniPrimary (citable) accession number: Q5R880
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: October 29, 2014
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3